메뉴 건너뛰기




Volumn 87, Issue 1, 2013, Pages 314-326

Mechanism for active membrane fusion triggering by morbillivirus attachment protein

Author keywords

[No Author keywords available]

Indexed keywords

EPITOPE; FUSION GLYCOPROTEIN; MONOCLONAL ANTIBODY; UNCLASSIFIED DRUG; VIRUS HEMAGGLUTININ; VIRUS PROTEIN;

EID: 84872002652     PISSN: 0022538X     EISSN: 10985514     Source Type: Journal    
DOI: 10.1128/JVI.01826-12     Document Type: Article
Times cited : (52)

References (71)
  • 5
    • 78049490873 scopus 로고    scopus 로고
    • Blue native PAGE and biomolecular complementation reveal a tetrameric or higher-order oligomer organization of the physiological measles virus attachment protein H
    • Brindley MA, Plemper RK. 2010. Blue native PAGE and biomolecular complementation reveal a tetrameric or higher-order oligomer organization of the physiological measles virus attachment protein H. J. Virol. 84:12174-12184.
    • (2010) J. Virol. , vol.84 , pp. 12174-12184
    • Brindley, M.A.1    Plemper, R.K.2
  • 8
    • 0027426010 scopus 로고
    • The human CD46 molecule is a receptor for measles virus (Edmonston strain)
    • Dorig RE, Marcil A, Chopra A, Richardson CD. 1993. The human CD46 molecule is a receptor for measles virus (Edmonston strain). Cell 75:295- 305.
    • (1993) Cell , vol.75
    • Dorig, R.E.1    Marcil, A.2    Chopra, A.3    Richardson, C.D.4
  • 11
    • 0034710650 scopus 로고    scopus 로고
    • SLAM (CDw150) is a cellular receptor for measles virus
    • Tatsuo H, Ono N, Tanaka K, Yanagi Y. 2000. SLAM (CDw150) is a cellular receptor for measles virus. Nature 406:893- 897.
    • (2000) Nature , vol.406
    • Tatsuo, H.1    Ono, N.2    Tanaka, K.3    Yanagi, Y.4
  • 12
    • 0034968597 scopus 로고    scopus 로고
    • Morbilliviruses use signaling lymphocyte activation molecules (CD150) as cellular receptors
    • Tatsuo H, Ono N, Yanagi Y. 2001. Morbilliviruses use signaling lymphocyte activation molecules (CD150) as cellular receptors. J. Virol. 75:5842- 5850.
    • (2001) J. Virol. , vol.75
    • Tatsuo, H.1    Ono, N.2    Yanagi, Y.3
  • 13
    • 33645456588 scopus 로고    scopus 로고
    • Role of sialic acid-containing molecules in paramyxovirus entry into the host cell: a minireview
    • Villar E, Barroso IM. 2006. Role of sialic acid-containing molecules in paramyxovirus entry into the host cell: a minireview. Glycoconj. J. 23:5-17.
    • (2006) Glycoconj. J. , vol.23 , pp. 5-17
    • Villar, E.1    Barroso, I.M.2
  • 17
    • 71949123985 scopus 로고    scopus 로고
    • Viral entry mechanisms: the increasing diversity of paramyxovirus entry
    • Smith EC, Popa A, Chang A, Masante C, Dutch RE. 2009. Viral entry mechanisms: the increasing diversity of paramyxovirus entry. FEBS J. 276: 7217-7227.
    • (2009) FEBS J. , vol.276 , pp. 7217-7227
    • Smith, E.C.1    Popa, A.2    Chang, A.3    Masante, C.4    Dutch, R.E.5
  • 18
    • 30144436116 scopus 로고    scopus 로고
    • Structure of the parainfluenza virus 5 F protein in its metastable, prefusion conformation
    • Yin HS, Wen X, Paterson RG, Lamb RA, Jardetzky TS. 2006. Structure of the parainfluenza virus 5 F protein in its metastable, prefusion conformation. Nature 439:38-44.
    • (2006) Nature , vol.439 , pp. 38-44
    • Yin, H.S.1    Wen, X.2    Paterson, R.G.3    Lamb, R.A.4    Jardetzky, T.S.5
  • 19
    • 79960387921 scopus 로고    scopus 로고
    • Structure of respiratory syncytial virus fusion glycoprotein in the postfusion conformation reveals preservation of neutralizing epitopes
    • McLellan JS, Yang Y, Graham BS, Kwong PD. 2011. Structure of respiratory syncytial virus fusion glycoprotein in the postfusion conformation reveals preservation of neutralizing epitopes. J. Virol. 85:7788-7796.
    • (2011) J. Virol. , vol.85 , pp. 7788-7796
    • Mclellan, J.S.1    Yang, Y.2    Graham, B.S.3    Kwong, P.D.4
  • 20
    • 77953021928 scopus 로고    scopus 로고
    • Structure of the Newcastle disease virus F protein in the post-fusion conformation
    • Swanson K, Wen X, Leser GP, Paterson RG, Lamb RA, Jardetzky TS. 2010. Structure of the Newcastle disease virus F protein in the post-fusion conformation. Virology 402:372-379.
    • (2010) Virology , vol.402 , pp. 372-379
    • Swanson, K.1    Wen, X.2    Leser, G.P.3    Paterson, R.G.4    Lamb, R.A.5    Jardetzky, T.S.6
  • 22
    • 0033762350 scopus 로고    scopus 로고
    • Crystal structure of the multifunctional paramyxovirus hemagglutinin-neuraminidase
    • Crennell S, Takimoto T, Portner A, Taylor G. 2000. Crystal structure of the multifunctional paramyxovirus hemagglutinin-neuraminidase. Nat. Struct. Biol. 7:1068-1074.
    • (2000) Nat. Struct. Biol. , vol.7 , pp. 1068-1074
    • Crennell, S.1    Takimoto, T.2    Portner, A.3    Taylor, G.4
  • 23
    • 0027430672 scopus 로고
    • Paramyxovirus fusion: a hypothesis for changes
    • Lamb RA. 1993. Paramyxovirus fusion: a hypothesis for changes. Virology 197:1-11.
    • (1993) Virology , vol.197 , pp. 1-11
    • Lamb, R.A.1
  • 25
    • 48249113696 scopus 로고    scopus 로고
    • Host cell recognition by the henipaviruses: crystal structures of the Nipah G attachment glycoprotein and its complex with ephrin-B3
    • Xu K, Rajashankar KR, Chan YP, Himanen JP, Broder CC, Nikolov DB. 2008. Host cell recognition by the henipaviruses: crystal structures of the Nipah G attachment glycoprotein and its complex with ephrin-B3. Proc. Natl. Acad. Sci. U. S. A. 105:9953-9958.
    • (2008) Proc. Natl. Acad. Sci. U. S. A. , vol.105 , pp. 9953-9958
    • Xu, K.1    Rajashankar, K.R.2    Chan, Y.P.3    Himanen, J.P.4    Broder, C.C.5    Nikolov, D.B.6
  • 26
    • 1842614339 scopus 로고    scopus 로고
    • Second sialic acid binding site in Newcastle disease virus hemagglutinin-neuraminidase: implications for fusion
    • Zaitsev V, von Itzstein M, Groves D, Kiefel M, Takimoto T, Portner A, Taylor G. 2004. Second sialic acid binding site in Newcastle disease virus hemagglutinin-neuraminidase: implications for fusion. J. Virol. 78:3733- 3741.
    • (2004) J. Virol. , vol.78
    • Zaitsev, V.1    von Itzstein, M.2    Groves, D.3    Kiefel, M.4    Takimoto, T.5    Portner, A.6    Taylor, G.7
  • 27
    • 59449099994 scopus 로고    scopus 로고
    • A novel receptor-induced activation site in the Nipah virus attachment glycoprotein (G) involved in triggering the fusion glycoprotein (F)
    • Aguilar HC, Ataman ZA, Aspericueta V, Fang AQ, Stroud M, Negrete OA, Kammerer RA, Lee B. 2009. A novel receptor-induced activation site in the Nipah virus attachment glycoprotein (G) involved in triggering the fusion glycoprotein (F). J. Biol. Chem. 284:1628-1635.
    • (2009) J. Biol. Chem. , vol.284 , pp. 1628-1635
    • Aguilar, H.C.1    Ataman, Z.A.2    Aspericueta, V.3    Fang, A.Q.4    Stroud, M.5    Negrete, O.A.6    Kammerer, R.A.7    Lee, B.8
  • 31
    • 0035941299 scopus 로고    scopus 로고
    • Measles virus envelope glycoproteins hetero-oligomerize in the endoplasmic reticulum
    • Plemper RK, Hammond AL, Cattaneo R. 2001. Measles virus envelope glycoproteins hetero-oligomerize in the endoplasmic reticulum. J. Biol. Chem. 276:44239-44246.
    • (2001) J. Biol. Chem. , vol.276 , pp. 44239-44246
    • Plemper, R.K.1    Hammond, A.L.2    Cattaneo, R.3
  • 32
    • 2342512265 scopus 로고    scopus 로고
    • Mutated form of the Newcastle disease virus hemagglutinin-neuraminidase interacts with the homologous fusion protein despite deficiencies in both receptor recognition and fusion promotion
    • Li J, Quinlan E, Mirza A, Iorio RM. 2004. Mutated form of the Newcastle disease virus hemagglutinin-neuraminidase interacts with the homologous fusion protein despite deficiencies in both receptor recognition and fusion promotion. J. Virol. 78:5299-5310.
    • (2004) J. Virol. , vol.78 , pp. 5299-5310
    • Li, J.1    Quinlan, E.2    Mirza, A.3    Iorio, R.M.4
  • 33
    • 0030680910 scopus 로고    scopus 로고
    • Paramyxovirus fusion (F) protein and hemagglutinin-neuraminidase (HN) protein interactions: intracellular retention of F and HN does not affect transport of the homotypic HN or F protein
    • Paterson RG, Johnson ML, Lamb RA. 1997. Paramyxovirus fusion (F) protein and hemagglutinin-neuraminidase (HN) protein interactions: intracellular retention of F and HN does not affect transport of the homotypic HN or F protein. Virology 237:1-9.
    • (1997) Virology , vol.237 , pp. 1-9
    • Paterson, R.G.1    Johnson, M.L.2    Lamb, R.A.3
  • 34
    • 84860234644 scopus 로고    scopus 로고
    • Paramyxovirus fusion and entry: multiple paths to a common end
    • Chang A, Dutch RE. 2012. Paramyxovirus fusion and entry: multiple paths to a common end. Viruses 4:613- 636.
    • (2012) Viruses , vol.4
    • Chang, A.1    Dutch, R.E.2
  • 35
    • 70350277403 scopus 로고    scopus 로고
    • Bimolecular complementation of paramyxovirus fusion and hemagglutininneuraminidase proteins enhances fusion: implications for the mechanism of fusion triggering
    • Connolly SA, Leser GP, Jardetzky TS, Lamb RA. 2009. Bimolecular complementation of paramyxovirus fusion and hemagglutininneuraminidase proteins enhances fusion: implications for the mechanism of fusion triggering. J. Virol. 83:10857-10868.
    • (2009) J. Virol. , vol.83 , pp. 10857-10868
    • Connolly, S.A.1    Leser, G.P.2    Jardetzky, T.S.3    Lamb, R.A.4
  • 36
    • 41549166734 scopus 로고    scopus 로고
    • Paramyxoviruses: different receptors- different mechanisms of fusion
    • Iorio RM, Mahon PJ. 2008. Paramyxoviruses: different receptors- different mechanisms of fusion. Trends Microbiol. 16:135-137.
    • (2008) Trends Microbiol. , vol.16 , pp. 135-137
    • Iorio, R.M.1    Mahon, P.J.2
  • 37
    • 79960918320 scopus 로고    scopus 로고
    • Modes of paramyxovirus fusion: a Henipavirus perspective
    • Lee B, Ataman ZA. 2011. Modes of paramyxovirus fusion: a Henipavirus perspective. Trends Microbiol. 19:389-399.
    • (2011) Trends Microbiol. , vol.19 , pp. 389-399
    • Lee, B.1    Ataman, Z.A.2
  • 38
    • 79959835596 scopus 로고    scopus 로고
    • Structural and mechanistic studies of measles virus illuminate paramyxovirus entry
    • doi:10.1371/journal.ppat.1002058
    • Plemper RK, Brindley MA, Iorio RM. 2011. Structural and mechanistic studies of measles virus illuminate paramyxovirus entry. PLoS Pathog. 7:e1002058. doi:10.1371/journal.ppat.1002058.
    • (2011) PLoS Pathog. , vol.7
    • Plemper, R.K.1    Brindley, M.A.2    Iorio, R.M.3
  • 39
    • 0038279845 scopus 로고    scopus 로고
    • Fusion deficiency induced by mutations at the dimer interface in the Newcastle disease virus hemagglutinin-neuraminidase is due to a temperaturedependent defect in receptor binding
    • Corey EA, Mirza AM, Levandowsky E, Iorio RM. 2003. Fusion deficiency induced by mutations at the dimer interface in the Newcastle disease virus hemagglutinin-neuraminidase is due to a temperaturedependent defect in receptor binding. J. Virol. 77:6913- 6922.
    • (2003) J. Virol. , vol.77
    • Corey, E.A.1    Mirza, A.M.2    Levandowsky, E.3    Iorio, R.M.4
  • 40
    • 8644256749 scopus 로고    scopus 로고
    • Amino acid substitutions in the F-specific domain in the stalk of the Newcastle disease virus HN protein modulate fusion and interfere with its interaction with the F protein
    • Melanson VR, Iorio RM. 2004. Amino acid substitutions in the F-specific domain in the stalk of the Newcastle disease virus HN protein modulate fusion and interfere with its interaction with the F protein. J. Virol. 78: 13053-13061.
    • (2004) J. Virol. , vol.78 , pp. 13053-13061
    • Melanson, V.R.1    Iorio, R.M.2
  • 41
    • 34247557393 scopus 로고    scopus 로고
    • Polybasic KKR motif in the cytoplasmic tail of Nipah virus fusion protein modulates membrane fusion by inside-out signaling
    • Aguilar HC, Matreyek KA, Choi DY, Filone CM, Young S, Lee B. 2007. Polybasic KKR motif in the cytoplasmic tail of Nipah virus fusion protein modulates membrane fusion by inside-out signaling. J. Virol. 81:4520- 4532.
    • (2007) J. Virol. , vol.81
    • Aguilar, H.C.1    Matreyek, K.A.2    Choi, D.Y.3    Filone, C.M.4    Young, S.5    Lee, B.6
  • 44
    • 35348888403 scopus 로고    scopus 로고
    • Mutations in the stalk of the measles virus hemagglutinin protein decrease fusion but do not interfere with virusspecific interaction with the homologous fusion protein
    • Corey EA, Iorio RM. 2007. Mutations in the stalk of the measles virus hemagglutinin protein decrease fusion but do not interfere with virusspecific interaction with the homologous fusion protein. J. Virol. 81: 9900-9910.
    • (2007) J. Virol. , vol.81 , pp. 9900-9910
    • Corey, E.A.1    Iorio, R.M.2
  • 45
    • 0036238643 scopus 로고    scopus 로고
    • Strength of envelope protein interaction modulates cytopathicity of measles virus
    • Plemper RK, Hammond AL, Gerlier D, Fielding AK, Cattaneo R. 2002. Strength of envelope protein interaction modulates cytopathicity of measles virus. J. Virol. 76:5051-5061.
    • (2002) J. Virol. , vol.76 , pp. 5051-5061
    • Plemper, R.K.1    Hammond, A.L.2    Gerlier, D.3    Fielding, A.K.4    Cattaneo, R.5
  • 46
    • 84855270854 scopus 로고    scopus 로고
    • Spring-loaded model revisited: paramyxovirus fusion requires engagement of a receptor binding protein beyond initial triggering of the fusion protein
    • Porotto M, DeVito I, Palmer SG, Jurgens EM, Yee JL, Yokoyama CC, Pessi A, Moscona A. 2011. Spring-loaded model revisited: paramyxovirus fusion requires engagement of a receptor binding protein beyond initial triggering of the fusion protein. J. Virol. 85:12867-12880.
    • (2011) J. Virol. , vol.85 , pp. 12867-12880
    • Porotto, M.1    Devito, I.2    Palmer, S.G.3    Jurgens, E.M.4    Yee, J.L.5    Yokoyama, C.C.6    Pessi, A.7    Moscona, A.8
  • 47
    • 84855272388 scopus 로고    scopus 로고
    • Mechanism of fusion triggering by human parainfluenza virus type III: communication between viral glycoproteins during entry
    • Porotto M, Palmer SG, Palermo LM, Moscona A. 2012. Mechanism of fusion triggering by human parainfluenza virus type III: communication between viral glycoproteins during entry. J. Biol. Chem. 287: 778-793.
    • (2012) J. Biol. Chem. , vol.287 , pp. 778-793
    • Porotto, M.1    Palmer, S.G.2    Palermo, L.M.3    Moscona, A.4
  • 48
    • 77953313394 scopus 로고    scopus 로고
    • Two domains of the V protein of virulent canine distemper virus selectively inhibit STAT1 and STAT2 nuclear import
    • Rothlisberger A, Wiener D, Schweizer M, Peterhans E, Zurbriggen A, Plattet P. 2010. Two domains of the V protein of virulent canine distemper virus selectively inhibit STAT1 and STAT2 nuclear import. J. Virol. 84:6328-6343.
    • (2010) J. Virol. , vol.84 , pp. 6328-6343
    • Rothlisberger, A.1    Wiener, D.2    Schweizer, M.3    Peterhans, E.4    Zurbriggen, A.5    Plattet, P.6
  • 49
    • 77957288876 scopus 로고    scopus 로고
    • Investigation of a unique short open reading frame within the 3= untranslated region of the canine distemper virus matrix messenger RNA
    • Wiener D, Vandevelde M, Zurbriggen A, Plattet P. 2010. Investigation of a unique short open reading frame within the 3= untranslated region of the canine distemper virus matrix messenger RNA. Virus Res. 153:234- 243.
    • (2010) Virus Res. , vol.153
    • Wiener, D.1    Vandevelde, M.2    Zurbriggen, A.3    Plattet, P.4
  • 50
    • 77953025370 scopus 로고    scopus 로고
    • Canine distemper virus persistence in demyelinating encephalitis by swift intracellular cell-to-cell spread in astrocytes is controlled by the viral attachment protein
    • Wyss-Fluehmann G, Zurbriggen A, Vandevelde M, Plattet P. 2010. Canine distemper virus persistence in demyelinating encephalitis by swift intracellular cell-to-cell spread in astrocytes is controlled by the viral attachment protein. Acta Neuropathol. 119:617- 630.
    • (2010) Acta Neuropathol. , vol.119
    • Wyss-fluehmann, G.1    Zurbriggen, A.2    Vandevelde, M.3    Plattet, P.4
  • 51
    • 77956029675 scopus 로고    scopus 로고
    • Identification of key residues in virulent canine distemper virus hemagglutinin that control CD150/SLAM-binding activity
    • Zipperle L, Langedijk JP, Orvell C, Vandevelde M, Zurbriggen A, Plattet P. 2010. Identification of key residues in virulent canine distemper virus hemagglutinin that control CD150/SLAM-binding activity. J. Virol. 84:9618-9624.
    • (2010) J. Virol. , vol.84 , pp. 9618-9624
    • Zipperle, L.1    Langedijk, J.P.2    Orvell, C.3    Vandevelde, M.4    Zurbriggen, A.5    Plattet, P.6
  • 52
    • 70349784080 scopus 로고    scopus 로고
    • Conserved leucine residue in the head region of morbillivirus fusion protein regulates the large conformational change during fusion activity
    • Plattet P, Langedijk JP, Zipperle L, Vandevelde M, Orvell C, Zurbriggen A. 2009. Conserved leucine residue in the head region of morbillivirus fusion protein regulates the large conformational change during fusion activity. Biochemistry 48:9112-9121.
    • (2009) Biochemistry , vol.48 , pp. 9112-9121
    • Plattet, P.1    Langedijk, J.P.2    Zipperle, L.3    Vandevelde, M.4    Orvell, C.5    Zurbriggen, A.6
  • 53
    • 0028129959 scopus 로고
    • Fusogenic mechanisms of enveloped-virus glycoproteins analyzed by a novel recombinant vaccinia virus-based assay quantitating cell fusion-dependent reporter gene activation
    • Nussbaum O, Broder CC, Berger EA. 1994. Fusogenic mechanisms of enveloped-virus glycoproteins analyzed by a novel recombinant vaccinia virus-based assay quantitating cell fusion-dependent reporter gene activation. J. Virol. 68:5411-5422.
    • (1994) J. Virol. , vol.68 , pp. 5411-5422
    • Nussbaum, O.1    Broder, C.C.2    Berger, E.A.3
  • 54
    • 35148875989 scopus 로고    scopus 로고
    • Signal peptide and helical bundle domains of virulent canine distemper virus fusion protein restrict fusogenicity
    • Plattet P, Cherpillod P, Wiener D, Zipperle L, Vandevelde M, Wittek R, Zurbriggen A. 2007. Signal peptide and helical bundle domains of virulent canine distemper virus fusion protein restrict fusogenicity. J. Virol. 81:11413-11425.
    • (2007) J. Virol. , vol.81 , pp. 11413-11425
    • Plattet, P.1    Cherpillod, P.2    Wiener, D.3    Zipperle, L.4    Vandevelde, M.5    Wittek, R.6    Zurbriggen, A.7
  • 55
    • 0029084129 scopus 로고
    • Non-replicating vaccinia vector efficiently expresses bacteriophage T7 RNA polymerase
    • Sutter G, Ohlmann M, Erfle V. 1995. Non-replicating vaccinia vector efficiently expresses bacteriophage T7 RNA polymerase. FEBS Lett. 371:9-12.
    • (1995) FEBS Lett. , vol.371 , pp. 9-12
    • Sutter, G.1    Ohlmann, M.2    Erfle, V.3
  • 56
    • 35348860151 scopus 로고    scopus 로고
    • Synergistic inhibition in cell-cell fusion mediated by the matrix and nucleocapsid protein of canine distemper virus
    • Wiener D, Plattet P, Cherpillod P, Zipperle L, Doherr MG, Vandevelde M, Zurbriggen A. 2007. Synergistic inhibition in cell-cell fusion mediated by the matrix and nucleocapsid protein of canine distemper virus. Virus Res. 129:145-154.
    • (2007) Virus Res. , vol.129 , pp. 145-154
    • Wiener, D.1    Plattet, P.2    Cherpillod, P.3    Zipperle, L.4    Doherr, M.G.5    Vandevelde, M.6    Zurbriggen, A.7
  • 57
    • 0033020645 scopus 로고    scopus 로고
    • Sequence analysis and expression of the attachment and fusion proteins of canine distemper virus wild-type strain A75/17
    • Cherpillod P, Beck K, Zurbriggen A, Wittek R. 1999. Sequence analysis and expression of the attachment and fusion proteins of canine distemper virus wild-type strain A75/17. J. Virol. 73:2263-2269.
    • (1999) J. Virol. , vol.73 , pp. 2263-2269
    • Cherpillod, P.1    Beck, K.2    Zurbriggen, A.3    Wittek, R.4
  • 58
    • 0021929252 scopus 로고
    • Preparation and characterization of monoclonal antibodies directed against four structural components of canine distemper virus
    • Orvell C, Sheshberadaran H, Norrby E. 1985. Preparation and characterization of monoclonal antibodies directed against four structural components of canine distemper virus. J. Gen. Virol. 66(Pt 3):443- 456.
    • (1985) J. Gen. Virol. 66(Pt , vol.3
    • Orvell, C.1    Sheshberadaran, H.2    Norrby, E.3
  • 59
    • 0025039308 scopus 로고
    • Contribution of measles virus fusion protein in protective immunity: anti-F monoclonal antibodies neutralize virus infectivity and protect mice against challenge
    • Malvoisin E, Wild F. 1990. Contribution of measles virus fusion protein in protective immunity: anti-F monoclonal antibodies neutralize virus infectivity and protect mice against challenge. J. Virol. 64:5160-5162.
    • (1990) J. Virol. , vol.64 , pp. 5160-5162
    • Malvoisin, E.1    Wild, F.2
  • 61
    • 34547770260 scopus 로고    scopus 로고
    • Reversible inhibition of the fusion activity of measles virus F protein by an engineered intersubunit disulfide bridge
    • Lee JK, Prussia A, Snyder JP, Plemper RK. 2007. Reversible inhibition of the fusion activity of measles virus F protein by an engineered intersubunit disulfide bridge. J. Virol. 81:8821- 8826.
    • (2007) J. Virol. , vol.81
    • Lee, J.K.1    Prussia, A.2    Snyder, J.P.3    Plemper, R.K.4
  • 66
    • 0034712879 scopus 로고    scopus 로고
    • Fusion protein of theparamyxovirus SV5: destabilizing and stabilizing mutants of fusion activation
    • Paterson RG, Russell CJ, Lamb RA. 2000. Fusion protein of theparamyxovirus SV5: destabilizing and stabilizing mutants of fusion activation. Virology 270:17-30.
    • (2000) Virology , vol.270 , pp. 17-30
    • Paterson, R.G.1    Russell, C.J.2    Lamb, R.A.3
  • 68
    • 18944375873 scopus 로고    scopus 로고
    • Structural studies of the parainfluenza virus 5 hemagglutinin- neuraminidase tetramer in complex with its receptor, sialyllactose
    • Yuan P, Thompson TB, Wurzburg BA, Paterson RG, Lamb RA, Jardetzky TS. 2005. Structural studies of the parainfluenza virus 5 hemagglutinin- neuraminidase tetramer in complex with its receptor, sialyllactose. Structure 13:803- 815.
    • (2005) Structure , vol.13
    • Yuan, P.1    Thompson, T.B.2    Wurzburg, B.A.3    Paterson, R.G.4    Lamb, R.A.5    Jardetzky, T.S.6
  • 69
    • 79955975776 scopus 로고    scopus 로고
    • Triggering of the Newcastle disease virus fusion protein by a chimeric attachment protein that binds to Nipah virus receptors
    • Mirza AM, Aguilar HC, Zhu Q, Mahon PJ, Rota PA, Lee B, Iorio RM. 2011. Triggering of the Newcastle disease virus fusion protein by a chimeric attachment protein that binds to Nipah virus receptors. J. Biol. Chem. 286:17851-17860.
    • (2011) J. Biol. Chem. , vol.286 , pp. 17851-17860
    • Mirza, A.M.1    Aguilar, H.C.2    Zhu, Q.3    Mahon, P.J.4    Rota, P.A.5    Lee, B.6    Iorio, R.M.7
  • 70
    • 79954628140 scopus 로고    scopus 로고
    • Resting lymphocyte transduction with measles virus glycoprotein pseudotyped lentiviral vectors relies on CD46 and SLAM
    • Zhou Q, Schneider IC, Gallet M, Kneissl S, Buchholz CJ. 2011. Resting lymphocyte transduction with measles virus glycoprotein pseudotyped lentiviral vectors relies on CD46 and SLAM. Virology 413:149-152.
    • (2011) Virology , vol.413 , pp. 149-152
    • Zhou, Q.1    Schneider, I.C.2    Gallet, M.3    Kneissl, S.4    Buchholz, C.J.5
  • 71
    • 33845212315 scopus 로고    scopus 로고
    • Refolding of a paramyxovirus F protein from prefusion to postfusion conformations observed by liposome binding and electron microscopy
    • Connolly SA, Leser GP, Yin HS, Jardetzky TS, Lamb RA. 2006. Refolding of a paramyxovirus F protein from prefusion to postfusion conformations observed by liposome binding and electron microscopy. Proc. Natl. Acad. Sci. U. S. A. 103:17903-17908.
    • (2006) Proc. Natl. Acad. Sci. U. S. A. , vol.103 , pp. 17903-17908
    • Connolly, S.A.1    Leser, G.P.2    Yin, H.S.3    Jardetzky, T.S.4    Lamb, R.A.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.